8fm1
From Proteopedia
(Difference between revisions)
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- | == | + | ==Structure of CBASS Cap5 from Pseudomonas syringae in the absence of a ligand (apo form dimer)== |
- | <StructureSection load='8fm1' size='340' side='right'caption='[[8fm1]]' scene=''> | + | <StructureSection load='8fm1' size='340' side='right'caption='[[8fm1]], [[Resolution|resolution]] 3.16Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FM1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FM1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[8fm1]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_syringae Pseudomonas syringae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FM1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FM1 FirstGlance]. <br> |
- | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.16Å</td></tr> |
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8fm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fm1 OCA], [https://pdbe.org/8fm1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fm1 RCSB], [https://www.ebi.ac.uk/pdbsum/8fm1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fm1 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8fm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fm1 OCA], [https://pdbe.org/8fm1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fm1 RCSB], [https://www.ebi.ac.uk/pdbsum/8fm1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fm1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/A0A2P0QGK5_PSESF A0A2P0QGK5_PSESF] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The bacterial cyclic oligonucleotide-based antiphage signaling system (CBASS) is similar to the cGAS-STING system in humans, containing an enzyme that synthesizes a cyclic nucleotide on viral infection and an effector that senses the second messenger for the antiviral response. Cap5, containing a SAVED domain coupled to an HNH DNA endonuclease domain, is the most abundant CBASS effector, yet the mechanism by which it becomes activated for cell killing remains unknown. We present here high-resolution structures of full-length Cap5 from Pseudomonas syringae (Ps) with second messengers. The key to PsCap5 activation is a dimer-to-tetramer transition, whereby the binding of second messenger to dimer triggers an open-to-closed transformation of the SAVED domains, furnishing a surface for assembly of the tetramer. This movement propagates to the HNH domains, juxtaposing and converting two HNH domains into states for DNA destruction. These results show how Cap5 effects bacterial cell suicide and we provide proof-in-principle data that the CBASS can be extrinsically activated to limit bacterial infections. | ||
+ | |||
+ | Activation of CBASS Cap5 endonuclease immune effector by cyclic nucleotides.,Rechkoblit O, Sciaky D, Kreitler DF, Buku A, Kottur J, Aggarwal AK Nat Struct Mol Biol. 2024 May;31(5):767-776. doi: 10.1038/s41594-024-01220-x. , Epub 2024 Feb 6. PMID:38321146<ref>PMID:38321146</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 8fm1" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Pseudomonas syringae]] |
+ | [[Category: Aggarwal AK]] | ||
+ | [[Category: Kreitler DF]] | ||
+ | [[Category: Rechkoblit O]] |
Current revision
Structure of CBASS Cap5 from Pseudomonas syringae in the absence of a ligand (apo form dimer)
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